Recombinant Mouse CDO His-tag Protein, CF

When Recombinant Mouse Sonic Hedgehog/Shh (C25II) N-Terminus (464-SH) is immobilized at 4 µg/mL (100 µL/well), Recombinant Mouse CDO His-tag (Catalog # 10505-CD) binds with an ED50 of 0.8-8 ng/mL.

2 μg/lane of Recombinant Mouse CDO His-tag Protein (10505-CD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 113-135 kDa.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse CDO His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse Sonic Hedgehog/Shh (C25II), N-Terminus (Catalog # 464-SH) is immobilized at 4 µg/mL (100 µL/well), Recombinant Mouse CDO His-tag (Catalog # 10505-CD) binds with an ED 50 of 0.8-8 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse CDO protein Asp25-Tyr962, with a C-terminal 6-His tag
• Accession #: Q32MD9.2
• N-terminal Sequence: Asp25
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 103 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 113-135 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse CDO His-tag Protein, CF

• CDO
• Cdon homolog (mouse)
• CDON
• CDOORCAM
• cell adhesion molecule-related/down-regulated by oncogenes
• MGC111524
• ORCAM
• surface glycoprotein, Ig superfamily member

Background

CAM-related/down-regulated by oncogene (CDO), also known as CDON is a member of the Ig/Fibronectin (FN) type III repeat family within the Ig superfamily. Mouse CDO is a type I transmembrane protein, consisting of a large extracellular domain (ECD), a transmembrane segment and a cytoplasmic region. The ECD contains five C2-type Ig-like domains, followed by three FN type III repeats (1). The first FN repeat is known to bind numerous cadherins, while the third (or juxtramembrane) FN type III repeat binds SHH (2, 3). The mature ECD of mouse CDO shares 85% amino acid identity to the ECD of human CDO. CDO is found on muscle precursor and neural progenitor cells of the embryo (4-6). It likely promotes muscle differentiation and contributes to axon guidance and neuronal patterning by signaling through various bHLH transcription factors (2, 5). These effects may be mediated through two different receptor complexes. On muscle precursors, CDO apparently acts as both a coordinating and signaling subunit. Here, it integrates N- and M-cadherin, neogenin, netrin-3 and BOC into a cis-oriented receptor complex (4, 7). While this complex has no identified ligand, intercellular cadherin interactions or netrin, may be enough to trigger CDO/cadherin/neogenin signaling. On axons, CDO may participate in a poorly-defined receptor complex minimally composed of CDO, BOC and Gas1 that binds SHH, and interacts with PTCH1 (8-10).

1. Kang, J.S. et al. (1997) J. Cell Biol. 138:203.
2. Yao, S. et al. (2006) Cell 125:343.
3. Kang, J-S. et al. (2003) Proc. Natl. Acad. Sci. USA 100:3989.
4. Kang, J-S. et al. (2002) EMBO J. 21:114.
5. Zhang, W. et al. (2006) Mol. Cell. Biol. 26:3764.
6. Krauss, R.S. et al. (2005) J. Cell Sci. 118:2355.
7. Kang, J-S. et al. (2004) J. Cell. Biol. 167:493.
8. Okada, A. et al. (2006) Nature 444:369.
9. Allen, B.L. et al. (2007) Genes Dev. 21:1244.
10. Tenzen, T. et al. (2006) Dev. Cell 10:647.

Bioinformatics

• Uniprot:
  • Q32MD9.2()